Cited by 308Mitochondrial Function and PathologyAutophagy in Disease and TherapyCellular transport and secretion

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A Role for Fis1 in Both Mitochondrial and Peroxisomal Fission in Mammalian Cells

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Koch, Annett, Yoon, Yisang, Bonekamp, Nina A., McNiven, Mark A., Schrader, Michael·2005·Molecular Biology of the Cell

DOI 10.1091/mbc.e05-02-0159PMC PMC1266408

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Abstract

The mammalian dynamin-like protein DLP1/Drp1 has been shown to mediate both mitochondrial and peroxisomal fission. In this study, we have examined whether hFis1, a mammalian homologue of yeast Fis1, which has been shown to participate in mitochondrial fission by an interaction with DLP1/Drp1, is also involved in peroxisomal growth and division. We show that hFis1 localizes to peroxisomes in addition to mitochondria. Through differential tagging and deletion experiments, we demonstrate that the transmembrane domain and the short C-terminal tail of hFis1 is both necessary and sufficient for its targeting to peroxisomes and mitochondria, whereas the N-terminal region is required for organelle fission. hFis1 promotes peroxisome division upon ectopic expression, whereas silencing of Fis1 by small interfering RNA inhibited fission and caused tubulation of peroxisomes. These findings provide the first evidence for a role of Fis1 in peroxisomal fission and suggest that the fission machinery of mitochondria and peroxisomes shares common components.

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Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
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BIOCHEMISTRY OF PEROXISOMES
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The Mitochondrial Protein hFis1 Regulates Mitochondrial Fission in Mammalian Cells through an Interaction with the Dynamin-Like Protein DLP1
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Authors: Koch, A., Yoon, Y., Bonekamp, N. A., McNiven, M. A., & Schrader, M.
Affiliations: Philipps University of Marburg (DE)
University of Rochester Medicine (US)
Mayo Clinic (US)
ORCID: Yoon, Yisang
Bonekamp, Nina A.
McNiven, Mark A.
Schrader, Michael
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2005-11
Volume: 16
Issue: 11
Pages: 5077-5086
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.e05-02-0159
PMC: PMC1266408
OpenAlex: W2128023952
Cited by: 308
References: 42
Citations by year: 2026: 8 · 2025: 8 · 2024: 13 · 2023: 13 · 2022: 16 · 2021: 8 · 2020: 17 · 2019: 10 · 2018: 17 · 2017: 11 · 2016: 15 · 2015: 17 · 2014: 14 · 2013: 24 · 2012: 15
FWCI: 6.42
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Biology of the Cell (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Philipps-Universität Marburg
La Trobe University
Universität Heidelberg
Université de Genève
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: Fis1, mitochondrial fission, Drp1, dynamin-like protein, peroxisome division, peroxisome targeting, transmembrane domain, C-terminal tail, mammalian cells
MeSH terms: Animals, Chlorocebus aethiops, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Transfection, COS Cells, GTP Phosphohydrolases, Peroxisomes, Mitochondrial Proteins, Dynamins, RNA, Small Interfering, Cell Line, Tumor, Rats

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A Role for Fis1 in Both Mitochondrial and Peroxisomal Fission in Mammalian Cells

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